Oxytetracycline-Binding Properties of Streptococcus Lactis
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چکیده
منابع مشابه
Pyruvate kinase of Streptococcus lactis.
The kinetic properties of pyruvate kinase (ATP:pyruvate-phosphotransferase, EC 2.7.1.40) from Streptococcus lactis have been investigated. Positive homotropic kinetics were observed with phosphoenolpyruvate and adenosine 5'-diphosphate, resulting in a sigmoid relationship between reaction velocity and substrate concentrations. This relationship was abolished with an excess of the heterotropic e...
متن کاملExtracellular Proteinase of Streptococcus Lactis.
Williamson, W. T. (North Carolina State of the University of North Carolina, Raleigh), S. B. Tove, and M. L. Speck. Extracellular proteinase of Streptococcus lactis. J. Bacteriol. 87:49-53. 1964.-Streptococcus lactis was shown to produce an extracellular proteolytic enzyme(s). A 120-fold purification of the proteinase was obtained from the cell-free culture medium by ammonium sulfate fractionat...
متن کاملProperties and biotin content of purified preparations of the ornithinecitrulline enzyme of Streptococcus lactis.
Previous investigations have shown that biotin deficiency in Streptococcus lactis 8039 is associated with the loss in ability to convert ornithine and carbamyl phosphate to citrulline (1). Although protein synthesis in the presence of biotin was found to be necessary to restore completely the ornithine-citrulline enzyme activity of the biotin-deficient cells (2), a preliminary report on the bio...
متن کاملKinetic properties of a phosphate-bond-driven glutamate-glutamine transport system in Streptococcus lactis and Streptococcus cremoris.
In Streptococcus lactis ML3 and Streptococcus cremoris Wg2 the uptake of glutamate and glutamine is mediated by the same transport system, which has a 30-fold higher affinity for glutamine than for glutamate at pH 6.0. The apparent affinity constant for transport (KT) of glutamine is 2.5 +/- 0.3 microM, independent of the extracellular pH. The KTS for glutamate uptake are 3.5, 11.2, 77, and 120...
متن کاملIntracellular hexose-6-phosphate:phosphohydrolase from Streptococcus lactis: purification, properties, and function.
An intracellular hexose 6-phosphate:phosphohydrolase (EC 3.1.3.2) has been purified from Streptococcus lactis K1. Polyacrylamide disc gel electrophoresis of the purified enzyme revealed one major activity staining protein and one minor inactive band. The Mr determined by gel permeation chromatography was 36,500, but sodium dodecyl sulfate-polyacrylamide gel electrophoresis revealed a single pol...
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ژورنال
عنوان ژورنال: Journal of Dairy Science
سال: 1965
ISSN: 0022-0302
DOI: 10.3168/jds.s0022-0302(65)88404-1